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Literature summary for 1.6.3.1 extracted from

  • Li, X.J.; Grunwald, D.; Mathieu, J.; Morel, F.; Stasia, M.J.
    Crucial role of two potential cytosolic regions of Nox2, 191TSSTKTIRRS200 and 484DESQANHFAVHHDEEKD500, on NADPH oxidase activation (2005), J. Biol. Chem., 280, 14962-14973.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D484T mutant of the alpha-helical loop of isoform Nox2, neither NADPH oxidase nor iodonitrotetrazolium reductase activity Homo sapiens
D500A mutant of the alpha-helical loop of isoform Nox2, neither NADPH oxidase nor iodonitrotetrazolium reductase activity Homo sapiens
D500G mutant of the alpha-helical loop of isoform Nox2, neither NADPH oxidase nor iodonitrotetrazolium reductase activity Homo sapiens
D500R mutant of the alpha-helical loop of isoform Nox2, neither NADPH oxidase nor iodonitrotetrazolium reductase activity Homo sapiens
K195A mutation in D-loop of isoform Nox2, complete loss of enzymic activity, but normal p47phox translocation and normal iodonitrotetrazolium reductase activity Homo sapiens
K195E mutation in D-loop of isoform Nox2, complete loss of enzymic activity, but normal p47phox translocation and normal iodonitrotetrazolium reductase activity Homo sapiens
additional information replacement of D-loop of isoform Nox2 with the homolog of Nox1, Nox3, or Nox4 is fully functional. Formylmethionine-activated mutant D-loopNox4 in Nox2 shows 4- to 8fold higher activity than wild-type Homo sapiens
R198A/R198A mutation in D-loop of isoform Nox2, complete loss of enzymic activity, but normal p47phox translocation and normal iodonitrotetrazolium reductase activity Homo sapiens
R198Q/R199Q mutation in D-loop of isoform Nox2, complete loss of enzymic activity, but normal p47phox translocation and normal iodonitrotetrazolium reductase activity Homo sapiens
R199E mutation in D-loop of isoform Nox2, complete loss of enzymic activity, but normal p47phox translocation and normal iodonitrotetrazolium reductase activity Homo sapiens
R199Q mutation in D-loop of isoform Nox2. Formylmethionine-activated mutant shows 4- to 8fold higher activity than wild-type Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isoform Nox2, reconmbinant enzyme
-

Subunits

Subunits Comment Organism
More the alpha-helical loop of isoform Nox2 is probably involved in the correct assembly of the NADPH oxidase complex, permitting cytosolic factor translocation and electron transfer from NADPH to FAD Homo sapiens